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Conserved domains on  [gi|1624158676|gb|THU61030|]
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hypothetical protein C4D60_Mb07t18980 [Musa balbisiana]

Protein Classification

DUF1929 domain-containing protein( domain architecture ID 12073925)

DUF1929 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 48-288 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


:

Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 516.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676  48 MHMQLLHNDRVVVFDRTDFGPSNLSLPDGRCRNDPNDKALPVDCTAHSAEYDVVANAFRPLMILTDTWCSSGSVAPDGTL 127
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 128 VQTGGFNDGERAARTFRPCDDGSCDWVETAQALAVRRWYATNQVLPDGRAVVVGGRRQFNYEFYPKPDPSDMSTIALRFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 208 QDTRDDVEDNLYPFVHLSIDGNLFIFANNRAILLDYSKNTVVRTYPKMPsGEPRNYPSSGSSVLLPLK---PSPTEAEVL 284
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLP-GGPRNYPSSGSSVLLPLDlnnDGFIEAEVL 239


                  ....
gi 1624158676 285 ICGG 288
Cdd:pfam07250 240 VCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 578-680 7.78e-29

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


:

Pssm-ID: 199882  Cd Length: 103  Bit Score: 110.41  E-value: 7.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 578 NSRLRPQILTPPSpiQLTYGGRFSLQFSVGVVseGGIRVTMVAPSFATHSFSMNQRLLVLE--TEGGTSEVVAVAPASDI 655
Cdd:cd02851     2 FGAPRPTITSAPK--TVGYGQTFTVTVSGPGG--GIVRVTLVRPGFVTHSFNMGQRLVKLPvtGSGGDYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 1624158676 656 LAPPGYYMVYVVNGE-VPSEGIWAHI 680
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 48-288 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 516.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676  48 MHMQLLHNDRVVVFDRTDFGPSNLSLPDGRCRNDPNDKALPVDCTAHSAEYDVVANAFRPLMILTDTWCSSGSVAPDGTL 127
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 128 VQTGGFNDGERAARTFRPCDDGSCDWVETAQALAVRRWYATNQVLPDGRAVVVGGRRQFNYEFYPKPDPSDMSTIALRFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 208 QDTRDDVEDNLYPFVHLSIDGNLFIFANNRAILLDYSKNTVVRTYPKMPsGEPRNYPSSGSSVLLPLK---PSPTEAEVL 284
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLP-GGPRNYPSSGSSVLLPLDlnnDGFIEAEVL 239


                  ....
gi 1624158676 285 ICGG 288
Cdd:pfam07250 240 VCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 578-680 7.78e-29

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 110.41  E-value: 7.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 578 NSRLRPQILTPPSpiQLTYGGRFSLQFSVGVVseGGIRVTMVAPSFATHSFSMNQRLLVLE--TEGGTSEVVAVAPASDI 655
Cdd:cd02851     2 FGAPRPTITSAPK--TVGYGQTFTVTVSGPGG--GIVRVTLVRPGFVTHSFNMGQRLVKLPvtGSGGDYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 1624158676 656 LAPPGYYMVYVVNGE-VPSEGIWAHI 680
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 589-680 5.42e-28

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 107.65  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 589 PSPIQLTYGGRFSLQFSVGvvseGGIRVTMVAPSFATHSFSMNQRLLVLE---TEGGTSEVVAVAPASDILAPPGYYMVY 665
Cdd:pfam09118   1 APPTTLSYGGTFTVTFGVA----GNVKVSLIRPGFVTHSVNMGQRLVFLDvtsTGGTGYTVTVTAPPNPNIAPPGYYMLF 76

                          90
                  ....*....|....*
gi 1624158676 666 VVNGEVPSEGIWAHI 680
Cdd:pfam09118  77 VVDNGVPSVGKWVRV 91
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
92-184 7.48e-04

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 42.07  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676  92 TAHSAEYDVVANAFRPLMILTDTWCSSGSVAPDGTLVQTGGFNDGERAARTFRpCDDGSCDWvETAQALAVRRWYATNQV 171
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEV-YDPATGTW-TQLAPLPTPRDHLAAAV 166

                          90
                  ....*....|...
gi 1624158676 172 LPDGRAVVVGGRR 184
Cdd:COG3055   167 LPDGKILVIGGRN 179
 
Name Accession Description Interval E-value
Glyoxal_oxid_N pfam07250
Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) ...
 48-288 0e+00

Glyoxal oxidase N-terminus; This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.


Pssm-ID: 399910 [Multi-domain]  Cd Length: 243  Bit Score: 516.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676  48 MHMQLLHNDRVVVFDRTDFGPSNLSLPDGRCRNDPNDKALPVDCTAHSAEYDVVANAFRPLMILTDTWCSSGSVAPDGTL 127
Cdd:pfam07250   1 MHMQLLHNNKVIMFDRTDFGPSNLSLPNGRCRNDPRDKALKTDCTAHSVEYDVATNTVRPLTILTDTWCSSGAFLPDGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 128 VQTGGFNDGERAARTFRPCDDGSCDWVETAQALAVRRWYATNQVLPDGRAVVVGGRRQFNYEFYPKPDPSDMSTIALRFL 207
Cdd:pfam07250  81 VQTGGFNDGERKVRYFSPCDSGTCDWVELPNGLAAGRWYATNQILPDGRVIVVGGRRAFSYEFVPKEGQSNEGVFELPFL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 208 QDTRDDVEDNLYPFVHLSIDGNLFIFANNRAILLDYSKNTVVRTYPKMPsGEPRNYPSSGSSVLLPLK---PSPTEAEVL 284
Cdd:pfam07250 161 RETNDPQENNLYPFVHLLPDGNLFIFANNRSILLDYKTNKVVREFPTLP-GGPRNYPSSGSSVLLPLDlnnDGFIEAEVL 239


                  ....
gi 1624158676 285 ICGG 288
Cdd:pfam07250 240 VCGG 243
E_set_GO_C cd02851
C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or ...
 578-680 7.78e-29

C-terminal Early set domain associated with the catalytic domain of galactose oxidase; E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199882  Cd Length: 103  Bit Score: 110.41  E-value: 7.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 578 NSRLRPQILTPPSpiQLTYGGRFSLQFSVGVVseGGIRVTMVAPSFATHSFSMNQRLLVLE--TEGGTSEVVAVAPASDI 655
Cdd:cd02851     2 FGAPRPTITSAPK--TVGYGQTFTVTVSGPGG--GIVRVTLVRPGFVTHSFNMGQRLVKLPvtGSGGDYTVTVTAPPNAN 77

                          90       100
                  ....*....|....*....|....*.
gi 1624158676 656 LAPPGYYMVYVVNGE-VPSEGIWAHI 680
Cdd:cd02851    78 VAPPGYYMLFVVNADgVPSVAKWVRV 103
GO-like_E_set pfam09118
Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the ...
 589-680 5.42e-28

Galactose oxidase-like, Early set domain; E or 'early' set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates, and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active centre necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end, and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. This domain is found in sugar-utilizing enzymes, such as galactose oxidase or chitinase.


Pssm-ID: 462683  Cd Length: 91  Bit Score: 107.65  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676 589 PSPIQLTYGGRFSLQFSVGvvseGGIRVTMVAPSFATHSFSMNQRLLVLE---TEGGTSEVVAVAPASDILAPPGYYMVY 665
Cdd:pfam09118   1 APPTTLSYGGTFTVTFGVA----GNVKVSLIRPGFVTHSVNMGQRLVFLDvtsTGGTGYTVTVTAPPNPNIAPPGYYMLF 76

                          90
                  ....*....|....*
gi 1624158676 666 VVNGEVPSEGIWAHI 680
Cdd:pfam09118  77 VVDNGVPSVGKWVRV 91
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
92-184 7.48e-04

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 42.07  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624158676  92 TAHSAEYDVVANAFRPLMILTDTWCSSGSVAPDGTLVQTGGFNDGERAARTFRpCDDGSCDWvETAQALAVRRWYATNQV 171
Cdd:COG3055    89 LNDVYVYDPATNTWTKLAPMPTPRGGATALLLDGKIYVVGGWDDGGNVAWVEV-YDPATGTW-TQLAPLPTPRDHLAAAV 166

                          90
                  ....*....|...
gi 1624158676 172 LPDGRAVVVGGRR 184
Cdd:COG3055   167 LPDGKILVIGGRN 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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